| Autor: |
Limjuco, G, Galuska, S, Chin, J, Cameron, P, Boger, J, Schmidt, J A |
| Zdroj: |
Proceedings of the National Academy of Sciences of the United States of America; June 1986, Vol. 83 Issue: 11 p3972-3976, 5p |
| Abstrakt: |
The development of highly specific antisera to human interleukin 1 (IL-1) has been an elusive goal hampered mainly by the availability of only limited amounts of pure immunogen. To surmount this difficulty, three peptides of the major charged species of IL-1 (pI 6.8) were synthesized and covalently coupled to keyhole limpet hemocyanin (KLH). All three peptide-KLH conjugates raised rabbit heterologous antisera that bound intact pure IL-1 in a dose-dependent and domain-specific manner. Immunoblot analysis of crude concentrated culture supernatants with these antisera showed each of them to be highly specific for mature 18-kDa IL-1. Immunoblot analysis of monocyte lysates revealed a single 33-kDa band consistent with the size of the IL-1 precursor molecule deduced from cloned cDNA. These reagents should prove to be valuable tools in the localization and measurement of IL-1 in cells and fluids and may permit the separate study of individual IL-1 species as well as discrete domains of intact IL-1 molecules. |
| Databáze: |
Supplemental Index |
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